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Protein

Protein arg11, mitochondrial

Gene

arg11

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH.
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate.

Enzyme regulationi

The kinase activity is inhibited by arginine.

Pathwayi: L-arginine biosynthesis

This protein is involved in step 2 and 3 of the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Arginine biosynthesis bifunctional protein ArgJ, mitochondrial (SPBC1271.14), Amino-acid acetyltransferase, mitochondrial (arg6)
  2. Protein arg11, mitochondrial (arg11)
  3. Protein arg11, mitochondrial (arg11)
  4. Probable acetylornithine aminotransferase, mitochondrial (arg1)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei703 – 7031PROSITE-ProRule annotation

GO - Molecular functioni

  • acetyl-CoA:L-glutamate N-acetyltransferase activity Source: GO_Central
  • acetylglutamate kinase activity Source: PomBase
  • arginine binding Source: GO_Central
  • ATP binding Source: UniProtKB-KW
  • N-acetyl-gamma-glutamyl-phosphate reductase activity Source: PomBase
  • NAD binding Source: InterPro

GO - Biological processi

  • arginine biosynthetic process Source: PomBase
  • ornithine biosynthetic process Source: PomBase

Keywords - Molecular functioni

Kinase, Oxidoreductase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Keywords - Ligandi

ATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00068; UER00107.
UPA00068; UER00108.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arg11, mitochondrial
Cleaved into the following 2 chains:
Alternative name(s):
N-acetyl-glutamate semialdehyde dehydrogenase
Short name:
NAGSA dehydrogenase
Alternative name(s):
N-acetyl-L-glutamate 5-phosphotransferase
NAG kinase
Short name:
AGK
Gene namesi
Name:arg11
ORF Names:SPAC4G9.09c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC4G9.09c.
PomBaseiSPAC4G9.09c. arg11.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: PomBase
  • mitochondrion Source: PomBase

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5959MitochondrionSequence analysisAdd
BLAST
Chaini60 – 550491Acetylglutamate kinaseSequence analysisPRO_0000002071Add
BLAST
Chaini551 – 885335N-acetyl-gamma-glutamyl-phosphate reductaseSequence analysisPRO_0000002072Add
BLAST

Post-translational modificationi

The protein precursor is cleaved into the two biologically active enzymes, the kinase and the reductase.

Keywords - PTMi

Cleavage on pair of basic residues

Proteomic databases

MaxQBiP31318.

Interactioni

Protein-protein interaction databases

BioGridi279813. 44 interactions.
MINTiMINT-4688310.

Structurei

3D structure databases

ProteinModelPortaliP31318.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini346 – 499154N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the acetylglutamate kinase family.Curated
In the C-terminal section; belongs to the NAGSA dehydrogenase family.Curated
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000201928.
InParanoidiP31318.
KOiK12659.
OMAiDENRAWH.
OrthoDBiEOG74TX88.
PhylomeDBiP31318.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR004662. AcgluKinase.
IPR023013. AGPR_AS.
IPR000706. AGPR_type-1.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR016040. NAD(P)-bd_dom.
IPR011241. NAGK_NAGSA.
IPR000534. Semialdehyde_DH_NAD-bd.
IPR006855. Vertebrate-like_GNAT_dom.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF04768. NAT. 1 hit.
PF01118. Semialdhyde_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF036440. ARG5-6. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00761. argB. 1 hit.
TIGR01850. argC. 1 hit.
PROSITEiPS01224. ARGC. 1 hit.
PS51731. GNAT_NAGS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31318-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIELQQIVK SGLVRNGAKH CTKRSLLCSN ASVIASKRFQ GSFAPGQQQP
60 70 80 90 100
LNPLAKPIEQ DRDAIIRILS SIGSRREVEQ YLRYFTSFEA QRFAIIKVGG
110 120 130 140 150
AIITDELDTL AQSLAFLNHV GLYPIVVHGA GPQLNKILAS RNVEPEYSDG
160 170 180 190 200
IRITDAETLS VARKVFLEEN AKLVDALEKL GTRARPITGG VFQAEYLDKE
210 220 230 240 250
KYKYVGKIVK VNKAPIEHSI RAGTLPILTS MAETASGQLL NVNADITAGE
260 270 280 290 300
LARVLKPLKV VYLNEKGGLI NGETKKKISS IYLDREYDGL MKQPWVKYGT
310 320 330 340 350
KLKIKEIKEL LDTLPRTSSV AIISTKDLQK ELFTESGAGT LISRGFVINK
360 370 380 390 400
HDSLDSIPDA ALENLIIQKN SLAAPSESLK QFKDTLKDRK LRIYSDSFNE
410 420 430 440 450
SVAIVDTTDS SLPVLLAFGA ADNNWLNNVV DSILTTLKAD FPSLLWRLQP
460 470 480 490 500
SAKNLEWFFS KSEGTLFANN FYYFWYGVKD LNKISKFIQS DKPFADAIIQ
510 520 530 540 550
TQSTKPPTAS STTNNPSSSQ INQKRSYSTS SLFSKNKKMN RSLFLKGGKR
560 570 580 590 600
FFSAEAQKTQ KPLKAVSSKP AKVVLLGARG YTGKNLIGLI NTHPYLELSH
610 620 630 640 650
VSSRELEGTK LPGYTKKEIQ YVNLSTDDVK KLEEEGAVDA WVMALPNGVC
660 670 680 690 700
KPYVDALTSA NGKSVIVDLS ADYRFEPSWQ YGLPELNDRE ALRNSKRISN
710 720 730 740 750
PGCYATGSQV GLTPILSLID GQPSIFGVSG YSGAGTKPSP KNDLNVLTNN
760 770 780 790 800
LIPYSLTDHI HEREISYRLK QPVAFIPHVA QWFQGITLTI NVPLKKSITS
810 820 830 840 850
RELRNLYQDR YNGEPLIHVQ GDVPLVKDNA HKHHVSVGGF GVHSSGKRAV
860 870 880
IVVTIDNLLK GAATQALQNL NLSCGYDEYA GIHLD
Length:885
Mass (Da):97,705
Last modified:October 1, 1996 - v2
Checksum:i3AA1A5082431B118
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti261 – 2611V → D in strain: 975.
Natural varianti345 – 3451G → P in strain: 975.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63576 Genomic DNA. Translation: CAA45132.1.
CU329670 Genomic DNA. Translation: CAA93559.1.
PIRiS22389.
RefSeqiNP_593691.1. NM_001019123.2.

Genome annotation databases

EnsemblFungiiSPAC4G9.09c.1; SPAC4G9.09c.1:pep; SPAC4G9.09c.
GeneIDi2543391.
KEGGispo:SPAC4G9.09c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63576 Genomic DNA. Translation: CAA45132.1.
CU329670 Genomic DNA. Translation: CAA93559.1.
PIRiS22389.
RefSeqiNP_593691.1. NM_001019123.2.

3D structure databases

ProteinModelPortaliP31318.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279813. 44 interactions.
MINTiMINT-4688310.

Proteomic databases

MaxQBiP31318.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC4G9.09c.1; SPAC4G9.09c.1:pep; SPAC4G9.09c.
GeneIDi2543391.
KEGGispo:SPAC4G9.09c.

Organism-specific databases

EuPathDBiFungiDB:SPAC4G9.09c.
PomBaseiSPAC4G9.09c. arg11.

Phylogenomic databases

HOGENOMiHOG000201928.
InParanoidiP31318.
KOiK12659.
OMAiDENRAWH.
OrthoDBiEOG74TX88.
PhylomeDBiP31318.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00107.
UPA00068; UER00108.

Miscellaneous databases

PROiP31318.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR004662. AcgluKinase.
IPR023013. AGPR_AS.
IPR000706. AGPR_type-1.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR016040. NAD(P)-bd_dom.
IPR011241. NAGK_NAGSA.
IPR000534. Semialdehyde_DH_NAD-bd.
IPR006855. Vertebrate-like_GNAT_dom.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF04768. NAT. 1 hit.
PF01118. Semialdhyde_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF036440. ARG5-6. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00761. argB. 1 hit.
TIGR01850. argC. 1 hit.
PROSITEiPS01224. ARGC. 1 hit.
PS51731. GNAT_NAGS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequencing of arg3 and arg11 genes of Schizosaccharomyces pombe on a 10-kb DNA fragment. Heterologous expression and mitochondrial targeting of their translation products."
    van Huffel C., Dubois E., Messenguy F.
    Eur. J. Biochem. 205:33-43(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 38365 / 975.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiARG56_SCHPO
AccessioniPrimary (citable) accession number: P31318
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.